Enzymatic Surface Hydrolysis of PET: Effect of Structural Diversity on Kinetic Properties of Cutinases from Thermobifida

Enrique Herrero Acero, Doris Ribitsch, Georg Steinkellner, +11

Macromolecules

EngineeringKinetic PropertiesEnzyme ImmobilizationEnzymatic ModificationBiosynthesis +17

A New Esterase from Thermobifida halotolerans Hydrolyses Polyethylene Terephthalate (PET) and Polylactic Acid (PLA)

Doris Ribitsch, Enrique Herrero Acero, Katrin Julia Greimel, +8

Polymers

Bioorganic ChemistryEngineeringNew EsteraseOrganic ChemistryPolysaccharide +15

Fusion of Binding Domains to Thermobifida cellulosilytica Cutinase to Tune Sorption Characteristics and Enhancing PET Hydrolysis

Doris Ribitsch, Antonio Orcal Yebra, Sabine Zitzenbacher, +12

Biomacromolecules

Surface engineering of a cutinase from <i>Thermobifida cellulosilytica</i> for improved polyester hydrolysis

Enrique Herrero Acero, Doris Ribitsch, Anita Dellacher, +6

Biotechnology and Bioengineering

EngineeringAmino AcidsBio-based MaterialChemical BiologyEnzymatic Modification +18

Improving enzymatic polyurethane hydrolysis by tuning enzyme sorption

Caroline Gamerith, Enrique Herrero Acero, Alessandro Pellis, +12

Polymer Degradation and Stability

EngineeringBiocatalysisBiochemical EngineeringBiotechnologyEnzymatic Modification +3

PpEst is a novel PBAT degrading polyesterase identified by proteomic screening of Pseudomonas pseudoalcaligenes

Paal W. Wallace, Karolina Haernvall, Doris Ribitsch, +6

Applied Microbiology and Biotechnology

EngineeringBacteriologyMolecular BiologyProteomic ScreeningProteomic Technology +19

Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2

Amit Singh, Georg Steinkellner, Katharina Köchl, +2

Scientific Reports

Hydrolysis of synthetic polyesters by <i>Clostridium botulinum</i> esterases

Veronika Perz, Armin Baumschlager, Klaus Bleymaier, +10

Biotechnology and Bioengineering

VASCo: computation and visualization of annotated protein surface contacts

Georg Steinkellner, Robert Rader, Gerhard Thallinger, +2

BMC Bioinformatics

Identification of promiscuous ene-reductase activity by mining structural databases using active site constellations

Georg Steinkellner, Christian Gruber, Tea Pavkov‐Keller, +10

Nature Communications